PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 65-74 ATP binding cassette subfamily C member 1 Homo sapiens 78-82 15355964-4 2004 To determine whether the other eucaryotic ABC transporters use the strategy analogous to that in some bacterial ABC transporters, the aromatic Trp653 residue in NBD1 and the Tyr1302 residue in NBD2 of human multidrug resistance-associated protein 1 (MRP1) was mutated to either a different aromatic residue or a polar cysteine residue. Cysteine 318-326 ATP binding cassette subfamily C member 1 Homo sapiens 207-248 15355964-7 2004 Interestingly, although substitution of the aromatic Trp653 in NBD1 of MRP1 with a polar cysteine residue greatly decreases the affinity for ATP, the ATP-dependent LTC4 transport activities are much higher than that of wild-type MRP1, supporting our hypothesis that the increased release rate of the bound ATP from the mutated NBD1 facilitates the protein to start a new cycle of ATP-dependent solute transport. Cysteine 89-97 ATP binding cassette subfamily C member 1 Homo sapiens 71-75 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 65-74 ATP binding cassette subfamily C member 1 Homo sapiens 253-257 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 65-74 ATP binding cassette subfamily C member 1 Homo sapiens 253-257 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 237-240 ATP binding cassette subfamily C member 1 Homo sapiens 78-82 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 237-240 ATP binding cassette subfamily C member 1 Homo sapiens 253-257 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 237-240 ATP binding cassette subfamily C member 1 Homo sapiens 253-257 15623154-1 2004 MIANS, a sulfhydryl-reactive fluorescence, was used to label the cysteines of MRP1 (multidrug resistance protein), and the results indicated that an increase in fluorescence intensity and a large emission blue shift took place after two Cys residues of MRP1 reacted with MIANS, which demonstrated that labeled Cys residues in MRP1 reside in a relatively hydrophobic environment. Cysteine 310-313 ATP binding cassette subfamily C member 1 Homo sapiens 78-82 15623154-2 2004 The experimental results obtained from fluorescence resonance energy transfer further uncover that two Cys residues of MRP1 modified by MIANS located in the vicinity of its NBDs, of which one lies close to NBD1, and the other near NBD2. Cysteine 103-106 ATP binding cassette subfamily C member 1 Homo sapiens 119-123 15623154-4 2004 The collisional quenchers, acrylamide, l-, and Cs+ were used to assess local environments of MIANS bound to MRP1 and the results showed that the region around the MIANS-labeled cysteine is positively charged. Cysteine 177-185 ATP binding cassette subfamily C member 1 Homo sapiens 108-112 15623154-7 2004 Nucleotides can bind directly to NBDs, but drugs may react first with TMDs, which in turn alters the accessibility of the two Cys residues bound by MIANS and affects MRP1 ATPase activity, which is coupled with the transport of its substrates. Cysteine 126-129 ATP binding cassette subfamily C member 1 Homo sapiens 166-170 12235150-0 2002 Structural and functional consequences of mutating cysteine residues in the amino terminus of human multidrug resistance-associated protein 1. Cysteine 51-59 ATP binding cassette subfamily C member 1 Homo sapiens 100-141 12731862-0 2003 Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1). Cysteine 42-50 ATP binding cassette subfamily C member 1 Homo sapiens 142-147 14522917-5 2003 Pulse-chase labeling of MRP1 with (35)S-methionine and (35)S-cysteine and pulse-chase biotinylation of cell surface MRP1 suggests that membrane protein mislocalization is caused mainly by a defect of plasma membrane protein recycling, manifested also as a defect in acidification of lysosomes. Cysteine 61-69 ATP binding cassette subfamily C member 1 Homo sapiens 24-28 12235150-6 2002 We found that the amino terminus of human MRP1 has two cysteine residues (Cys(7) and Cys(32)) that are conserved among the five human MRPs that have MSD1. Cysteine 55-63 ATP binding cassette subfamily C member 1 Homo sapiens 42-46 12235150-6 2002 We found that the amino terminus of human MRP1 has two cysteine residues (Cys(7) and Cys(32)) that are conserved among the five human MRPs that have MSD1. Cysteine 74-77 ATP binding cassette subfamily C member 1 Homo sapiens 42-46 12235150-6 2002 We found that the amino terminus of human MRP1 has two cysteine residues (Cys(7) and Cys(32)) that are conserved among the five human MRPs that have MSD1. Cysteine 85-88 ATP binding cassette subfamily C member 1 Homo sapiens 42-46 12235150-7 2002 Mutation analyses of the two cysteines in human MRP1 revealed that the Cys(7) residue is critical for the MRP1-mediated drug resistance and leukotriene C(4) transport activity. Cysteine 29-38 ATP binding cassette subfamily C member 1 Homo sapiens 48-52 12235150-7 2002 Mutation analyses of the two cysteines in human MRP1 revealed that the Cys(7) residue is critical for the MRP1-mediated drug resistance and leukotriene C(4) transport activity. Cysteine 29-38 ATP binding cassette subfamily C member 1 Homo sapiens 106-110 12235150-7 2002 Mutation analyses of the two cysteines in human MRP1 revealed that the Cys(7) residue is critical for the MRP1-mediated drug resistance and leukotriene C(4) transport activity. Cysteine 71-74 ATP binding cassette subfamily C member 1 Homo sapiens 48-52 12235150-7 2002 Mutation analyses of the two cysteines in human MRP1 revealed that the Cys(7) residue is critical for the MRP1-mediated drug resistance and leukotriene C(4) transport activity. Cysteine 71-74 ATP binding cassette subfamily C member 1 Homo sapiens 106-110 12235150-8 2002 On the other hand, mutation of Cys(32) reduced only moderately the MRP1 function. Cysteine 31-34 ATP binding cassette subfamily C member 1 Homo sapiens 67-71 12235150-9 2002 The effect of Cys(7) mutation on MRP1 activity appears to be due to the 5-7-fold decrease in the maximal transport rate V(max). Cysteine 14-17 ATP binding cassette subfamily C member 1 Homo sapiens 33-37 12235150-10 2002 We also found that mutation of Cys(7) changed the amino-terminal conformation of MRP1. Cysteine 31-34 ATP binding cassette subfamily C member 1 Homo sapiens 81-85 12235150-12 2002 Based on these studies, we conclude that the amino terminus of human MRP1 is important and that the Cys(7) residue plays a critical role in maintaining the proper structure and function of human MRP1. Cysteine 100-103 ATP binding cassette subfamily C member 1 Homo sapiens 195-199 19788237-3 2009 A cysteine mimetic analogue of GSAO was made, PENAO, which accumulates in cells 85 times faster than GSAO due to increased rate of entry and decreased rate of export via MRP1/2. Cysteine 2-10 ATP binding cassette subfamily C member 1 Homo sapiens 170-176 8869738-4 1996 Substrates for MRP include thioether-linked conjugates of lipophilic compounds with glutathione, cysteinyl glycine, cysteine, and N-acetyl cysteine, but also glutathione disulfide, and glucuronate conjugates such as etoposide glucuronide. Cysteine 116-124 ATP binding cassette subfamily C member 1 Homo sapiens 15-18 32055360-3 2019 Moreover, with the probe, a possible self-protection mechanism of cancer cells was indicated: when extracellular Cys sources are blocked, cancer cells could still survive by multidrug resistance protein transporter (Mrp1)-mediated export of intracellular GSH/GSSG as sources to supply intracellular Cys for resisting detrimental oxidative stress. Cysteine 113-116 ATP binding cassette subfamily C member 1 Homo sapiens 216-220 32055360-3 2019 Moreover, with the probe, a possible self-protection mechanism of cancer cells was indicated: when extracellular Cys sources are blocked, cancer cells could still survive by multidrug resistance protein transporter (Mrp1)-mediated export of intracellular GSH/GSSG as sources to supply intracellular Cys for resisting detrimental oxidative stress. Cysteine 299-302 ATP binding cassette subfamily C member 1 Homo sapiens 216-220 29572332-3 2018 Here, we report the first successful attempt using cysteine-scanning mutagenesis coupled with cross-linking studies to probe the structure of hMRP1 in its native environment of the cell membrane or in membrane vesicles. Cysteine 51-59 ATP binding cassette subfamily C member 1 Homo sapiens 142-147